4IOU

Crystal structure of the HIV-1 Vif binding, catalytically active domain of APOBEC3F

Summary for 4IOU

• Entry DOI: 10.2210/pdb4iou/pdb
• Descriptor: DNA dC->dU-editing enzyme APOBEC-3F, ZINC ION (3 entities in total)
• Functional Keywords: catalytic domain, cytidine deaminase, cytidine deaminase-like, hydrolase, dna binding, cytidine deamination
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 93109.38

Authors

Bohn, M.,Shandilya, S.M.D.,Schiffer, C.A. (deposition date: 2013-01-08, release date: 2013-05-29, Last modification date: 2023-09-20)

Primary citation

Bohn, M.F.,Shandilya, S.M.,Albin, J.S.,Kouno, T.,Anderson, B.D.,McDougle, R.M.,Carpenter, M.A.,Rathore, A.,Evans, L.,Davis, A.N.,Zhang, J.,Lu, Y.,Somasundaran, M.,Matsuo, H.,Harris, R.S.,Schiffer, C.A.
Crystal Structure of the DNA Cytosine Deaminase APOBEC3F: The Catalytically Active and HIV-1 Vif-Binding Domain.
Structure, 21:1042-1050, 2013

PubMed Abstract: Human APOBEC3F is an antiretroviral single-strand DNA cytosine deaminase, susceptible to degradation by the HIV-1 protein Vif. In this study the crystal structure of the HIV Vif binding, catalytically active, C-terminal domain of APOBEC3F (A3F-CTD) was determined. The A3F-CTD shares structural motifs with portions of APOBEC3G-CTD, APOBEC3C, and APOBEC2. Residues identified to be critical for Vif-dependent degradation of APOBEC3F all fit within a predominantly negatively charged contiguous region on the surface of A3F-CTD. Specific sequence motifs, previously shown to play a role in Vif susceptibility and virion encapsidation, are conserved across APOBEC3s and between APOBEC3s and HIV-1 Vif. In this structure these motifs pack against each other at intermolecular interfaces, providing potential insights both into APOBEC3 oligomerization and Vif interactions.

PubMed: 23685212
DOI: 10.1016/j.str.2013.04.010

Experimental method

X-RAY DIFFRACTION (2.751 Å)